Discarding functional residues from the substitution table improves predictions of active sites within three-dimensional structures

PLoS Computational Biology

Volumn 4, Issue 10, 2008, Pages

  Gong, Sungsam ^a   Blundell, Tom L ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; FORECASTING; HYDROGEN BONDS; NUCLEIC ACIDS; PROTEINS; SOFTWARE TESTING;

ACTIVE SITE; AMINO ACID SUBSTITUTION; AMINO-ACIDS; FUNCTIONAL RESIDUES; PATTERN OF SUBSTITUTION; PROTEIN-PROTEIN INTERACTIONS; SECONDARY STRUCTURES; SOLVENT ACCESSIBILITY; SUBSTITUTION TABLES; THREE-DIMENSIONAL STRUCTURE;

AMINO ACIDS;

AMINO ACID; ENZYME; LIGAND; NUCLEIC ACID; PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; ENZYME ACTIVITY; PROTEIN FUNCTION; PROTEIN NUCLEIC ACID INTERACTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; BIOLOGY; CHEMISTRY; COMPUTER PROGRAM; ENZYME ACTIVE SITE; GENETICS; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN ANALYSIS; PROTEIN DATABASE; SEQUENCE ALIGNMENT; STATISTICS;

AMINO ACID SUBSTITUTION; BINDING SITES; CATALYTIC DOMAIN; COMPUTATIONAL BIOLOGY; CONSERVED SEQUENCE; DATABASES, PROTEIN; ENZYMES; LIGANDS; NUCLEIC ACIDS; PROTEIN INTERACTION MAPPING; PROTEINS; SEQUENCE ALIGNMENT; SOFTWARE;

EID: 55449117336     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000179     Document Type: Article

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